| 2009 |
Yju2 is required for the first catalytic step of splicing after the action of Prp2, functioning at the final step of the first transesterification reaction. Cwc25 acts after Yju2 in the same step, and both are required for promoting juxtaposition of the 5' splice site and branch point. |
Depletion/reconstitution assay in yeast splicing extracts; ATP-independent rescue with recombinant protein |
Molecular and cellular biology |
High |
19704000
|
| 2009 |
Ntc90 (a component of the NineTeen Complex/NTC) is specifically required for recruiting Yju2 to the spliceosome after activation, but not for spliceosome activation itself, revealing a novel NTC role in recruiting first-step splicing factors. |
Biochemical fractionation, genetic deletion analysis, and reconstitution in yeast splicing extracts |
RNA (New York, N.Y.) |
High |
19617314
|
| 2010 |
Yju2 and Cwc25 are released from the spliceosome after the first catalytic step in a Prp16- and ATP-dependent manner, and this release is necessary to allow progression to the second catalytic reaction. |
Biochemical splicing assays with ATP/AMP-PNP, spliceosome purification, and factor addition/depletion in yeast extracts |
RNA (New York, N.Y.) |
High |
21098140
|
| 2012 |
High-affinity binding sites for Yju2 and Cwc25 are created on the spliceosome during Prp2-mediated catalytic activation (B* complex formation), consistent with their requirement for step 1 catalysis. |
Dual-color fluorescence cross-correlation spectroscopy (dcFCCS) on purified yeast spliceosomes |
RNA (New York, N.Y.) |
High |
22535589
|
| 2012 |
Ccdc94 (human ortholog of Yju2) is a functional member of the Prp19 complex, and knockdown of Prp19 complex members increases sensitivity to ionizing radiation-induced apoptosis; Ccdc94/Prp19 complex protects cells from IR-induced apoptosis by repressing p53 mRNA expression. |
Zebrafish forward genetic screen, genetic knockdown, RT-PCR for p53 mRNA levels, rescue experiments |
PLoS genetics |
Medium |
22952453
|
| 2013 |
Yju2 has a modular structure: the N-terminal half (Yju2-N) weakly binds the spliceosome and functions in the first step, while the C-terminal half (Yju2-C) stabilizes spliceosome association. Yju2-N alone supports a low level of the second reaction even without Prp16, suggesting that Prp16 acts primarily by destabilizing the C-domain-dependent tight spliceosome binding of Yju2. UV cross-linking shows Yju2 directly contacts U2 snRNA in helix II both pre- and post-catalytically, and contacts the branch-binding region only pre-catalytically. |
Domain dissection with in vivo and in vitro reconstitution, UV cross-linking to U2 snRNA, ATPase bypass assays in yeast |
Molecular and cellular biology |
High |
23438600
|
| 2006 |
FLJ10374 (YJU2/CCDC94) localizes exclusively to the nucleus and negatively regulates cell cycle G1-to-S transition; siRNA knockdown increases cell proliferation. |
Transfection with fluorescence localization, serum-starvation cell cycle assay, siRNA knockdown with proliferation readout |
Genes, chromosomes & cancer |
Medium |
16450356
|
| 2016 |
Cryo-EM structure of the C complex (post-branching) spliceosome at 3.8 Å shows that Yju2 (along with Isy1 and Cwc25) stabilizes docking of the branch helix, positioning the branch adenosine in the active site and facilitating the first transesterification reaction. |
Cryo-electron microscopy at 3.8 Å resolution of yeast C complex spliceosome |
Nature |
High |
27459055
|
| 2016 |
Cryo-EM structure at 3.4 Å of the yeast C complex confirms Yju2 is one of 15 protein components that stabilize specific placement of RNA elements (5'SS, BPS, U5 loop I) at the Prp8 catalytic cavity after the first transesterification reaction. |
Cryo-electron microscopy at 3.4 Å resolution of yeast C complex spliceosome |
Science (New York, N.Y.) |
High |
27445308
|
| 2016 |
Cryo-EM structure of the C* complex shows that the step I splicing factors Cwc25 and Yju2 have dissociated from the active site during the C-to-C* transition, vacating space for the incoming 3'-exon sequences required for the second transesterification. |
Cryo-electron microscopy at 4.0 Å resolution of yeast C* complex spliceosome |
Science (New York, N.Y.) |
High |
27980089
|
| 2018 |
Cryo-EM structure of the human C complex at 4.1 Å shows that CCDC94 (human Yju2) closely interacts with the DEAH-family ATPase/helicase Prp16 and bridges the gap between Prp16 and the active-site RNA elements, providing mechanistic insight into the C-to-C* transition. |
Cryo-electron microscopy at 4.1 Å resolution of human C complex spliceosome |
Science (New York, N.Y.) |
High |
29301961
|
| 2019 |
Cryo-EM structures of four B* complexes at 2.9–3.8 Å reveal that Yju2 recruitment into the active site brings the U2/BPS duplex into the vicinity of the 5' splice site, positioning the BPS nucleophile 4 Å from catalytic metal M2, directly demonstrating Yju2's mechanistic role in promoting the branching reaction. |
Cryo-electron microscopy of four yeast B* complexes at 2.9–3.8 Å, comparative structural analysis with and without Yju2/Cwc25 |
Cell |
High |
30879786
|
| 2021 |
Cryo-EM structure at 2.8 Å of the yeast C complex reveals that Yju2 and Isy1 are recruited to the spliceosome by the NTC before branching. After branching, Prp16 remodels Yju2 binding, allowing Yju2 to remain tethered to the NTC in the C* complex to promote exon ligation. |
Cryo-EM at 2.8 Å combined with biochemical assays for C/C* complex dynamics |
Molecular cell |
High |
33705709
|
| 2021 |
Rat1 exoribonuclease physically interacts with the Yju2 splicing factor (co-immunoprecipitation and mass spectrometry), and is required for proper co-transcriptional recruitment of splicing factors including Yju2 to introns. |
Co-immunoprecipitation, mass spectrometry, ChIP-Seq in yeast |
Nucleic acids research |
Medium |
33978753
|
| 2024 |
Cryo-EM structure of a yeast product complex spliceosome at 2.3 Å shows that binding of the second-step factor Fyv6 to the spliceosome is mutually exclusive with that of the first-step factor Yju2, and that Yju2/Fyv6 exchange facilitates progression from the first to the second step of splicing. |
Cryo-EM at 2.3 Å, genetic suppressor screen, transcriptomics |
eLife |
High |
39688371
|
| 2025 |
Molecular dynamics simulations integrating cryo-EM data reveal that Yju2 acts in a temporally ordered fashion with Prp11 and Prp8 at the spliceosome core, with positively charged residues in these proteins dynamically remodeling the active site to enable the first step of splicing. |
Equilibrium and enhanced sampling molecular dynamics simulations (>2M atoms) of multiple spliceosome structures |
Proceedings of the National Academy of Sciences of the United States of America |
Low |
41474748
|